Purification and partial amino acid sequence of annexin V from porcine gastric mucosal membranes Academic Article uri icon

abstract

  • 1. Annexin V has been purified from Triton X-100 extracts of porcine gastric mucosal membranes by a combination of chromatography on concanavalin A-Sepharose and DEAE-Sepharose, and preparative gel electrophoresis. 2. No N-terminal amino acid sequence was detected. 3. The sequences of 11 tryptic peptides were determined, amounting to a total of 121 amino acids, or 38% of the molecule. 4. When the peptides were compared with the cDNA-derived sequence of human annexin V, only three substitutions were observed. 5. Human and porcine annexin V are 97% homologous within the sequenced regions.

authors

  • Baldwin, Graham S
  • Moritz, Robert L
  • Rubira, Michael
  • Lin Seet, K
  • Weinstock, Janet
  • Simpson, Richard J

publication date

  • January 1991